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Three Mammalian Lipins Act as Phosphatidate Phosphatases with Distinct Tissue Expression Patterns*
TLDR
The results establish the three mammalian lipin proteins as PAP1 enzymes and explain the biochemical basis for lipodystrophy in the lipin-1-deficient fld mouse.
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(n-3) PUFA alter raft lipid composition and decrease epidermal growth factor receptor levels in lipid rafts of human breast cancer cells.
TLDR
The results indicate that (n-3) FA modify the lipid composition of membrane rafts and alter EGFR signaling in a way that decreases the growth of breast tumors.
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Mammalian Lipid Phosphate Phosphohydrolases*
TLDR
The PAP-2 family is proposed to be renamed as lipid phosphate phosphohydrolases (LPPs), based upon a lack of requirement for bivalent cations and insensitivity to inhibition by N-ethylmaleimide.
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High-fat feeding alters both basal and stress-induced hypothalamic-pituitary-adrenal activity in the rat.
TLDR
Dietary fat intake acts as a background form of chronic stress, elevating basal B levels and enhancing HPA responses to stress, suggesting support for the specificity of the effects on the HPA axis.
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Lipid phosphate phosphatases and related proteins: Signaling functions in development, cell division, and cancer
  • D. Brindley
  • Biology
    Journal of cellular biochemistry
  • 1 August 2004
TLDR
Observations imply that phosphatases that degrade lipid phosphates on the cell surface, or inside the cell, regulate cell signaling under physiological and pathological conditions.
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Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol.
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Lipid phosphate phosphatases and signaling The work was supported by the Canadian Institutes of Health Research. Published, JLR Papers in Press, December 9, 2008.
TLDR
The proposed integrin binding domain on the external surface of LPP3 modifies cell/cell interactions and expresses LPPs on internal membranes controls signaling depending on the access of lipid phosphates to their active sites.
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A Conserved Serine Residue Is Required for the Phosphatidate Phosphatase Activity but Not the Transcriptional Coactivator Functions of Lipin-1 and Lipin-2*
TLDR
The results indicate that the symptoms of the Majeed syndrome result from a loss of lipin-2 PAP activity, which may contribute to the anemia and inflammation phenotypes observed in Majeed Syndrome patients.
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The potential for treatment with dietary long-chain polyunsaturated n-3 fatty acids during chemotherapy.
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Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action.
TLDR
The present results demonstrate the active site to be located on the outer surface of mouse LPP-1, and the glycosylation site was demonstrated between conserved Domains 1 and 2.
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